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Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form

CITE Title : Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form Personal Author(s) : Vitu, Elvira;Sharma, Sapna;Stampfer, Samuel D.;Heldwein, Ekaterina E.; Published Date : March 13 2013;6-12-; Source : J Mol Biol. 2013; 425(11):2056-2071 URL : https://stacks.cdc.gov/view/cdc/29660 Vitu, Elvira et al. (2013). Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form. 425(11). Vitu, Elvira et al. "Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form" 425, no. 11 (2013) Vitu, Elvira et al. "Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form" vol. 425, no. 11, 2013 Export RIS Citation Information.

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Vitu, Elvira ;

Sharma, Sapna

March 13 2013 | J Mol Biol. 2013; 425(11):2056-2071

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Viral fusogens mediate the merger of the viral envelope and cellular membrane during viral entry. These proteins share little sequence similarity but ...
An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization

CITE Title : An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization Personal Author(s) : Britton, Zachary T.;Hanle, Elizabeth I.;Robinson, Anne S.; Published Date : 8 2012;8-2012; Source : Protein Expr Purif. 2012; 84(2):224-235 URL : https://stacks.cdc.gov/view/cdc/33517 Britton, Zachary T. et al. (2012). An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization. 84(2). Britton, Zachary T. and Hanle, Elizabeth I. and Robinson, Anne S. "An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization" 84, no. 2 (2012) Britton, Zachary T. et al. "An expression and purification system for the biosynthesis of adenosine receptor peptides for biophysical and structural characterization" vol. 84, no. 2, 2012 Export RIS Citation Information.

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Britton, Zachary T. ;

Hanle, Elizabeth I.

8 2012 | Protein Expr Purif. 2012; 84(2):224-235

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Biophysical and structural characterization of G protein-coupled receptors (GPCRs) has been limited due to difficulties in expression, purification, a...
Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center

CITE Title : Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center Personal Author(s) : Gil, Magdalena;Graña, Martín;Schopfer, Francisco J.;Wagner, Tristan;Denicola, Ana;Freeman, Bruce A.;Alzari, Pedro M.;Batthyány, Carlos;Durán, Rosario; Published Date : 12 2013;12-2013; Source : Free Radic Biol Med. 2013; 65:150-161 URL : https://stacks.cdc.gov/view/cdc/41966 Gil, Magdalena et al. (2013). Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center. 65 Gil, Magdalena et al. "Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center" 65 (2013) Gil, Magdalena et al. "Inhibition of Mycobacterium tuberculosis PknG by non-catalytic rubredoxin domain specific modification: reaction of an electrophilic nitro-fatty acid with the Fe–S center" vol. 65, 2013 Export RIS Citation Information.

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Gil, Magdalena ;

Graña, Martín

12 2013 | Free Radic Biol Med. 2013; 65:150-161

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PknG from Mycobacterium tuberculosis is a Ser/Thr protein kinase that regulates key metabolic processes within the bacterial cell as well as signaling...